Recommended Products
Quality Level
Assay
≥97.0% (GC)
refractive index
n20/D 1.423
density
1.176 g/mL at 20 °C (lit.)
functional group
carboxylic acid
ester
SMILES string
CC(OC(C)=O)C(O)=O
InChI
1S/C5H8O4/c1-3(5(7)8)9-4(2)6/h3H,1-2H3,(H,7,8)
InChI key
WTLNOANVTIKPEE-UHFFFAOYSA-N
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Analytical biochemistry, 342(1), 126-133 (2005-06-17)
Acetohydroxy acid synthase (AHAS) and related enzymes catalyze the production of chiral compounds [(S)-acetolactate, (S)-acetohydroxybutyrate, or (R)-phenylacetylcarbinol] from achiral substrates (pyruvate, 2-ketobutyrate, or benzaldehyde). The common methods for the determination of AHAS activity have shortcomings. The colorimetric method for detection
Bioorganic chemistry, 34(6), 380-393 (2006-11-07)
In addition to the decarboxylation of 2-oxo acids, thiamin diphosphate (ThDP)-dependent decarboxylases/dehydrogenases can also carry out so-called carboligation reactions, where the central ThDP-bound enamine intermediate reacts with electrophilic substrates. For example, the enzyme yeast pyruvate decarboxylase (YPDC, from Saccharomyces cerevisiae)
Applied and environmental microbiology, 62(7), 2636-2640 (1996-07-01)
Diacetyl is a by-product of pyruvate metabolism in Lactococcus lactis, where pyruvate is first converted to alpha-acetolactate, which is slowly decarboxylated to diacetyl in the presence of oxygen. L. lactis usually converts alpha-acetolactate to acetoin enzymatically, by alpha-acetolactate decarboxylase encoded
Proteins, 78(7), 1774-1788 (2010-03-13)
Acetohydroxyacid synthase (AHAS) is a thiamin diphosphate dependent enzyme that catalyses the decarboxylation of pyruvate to yield the hydroxyethyl-thiamin diphosphate (ThDP) anion/enamine intermediate (HEThDP(-)). This intermediate reacts with a second ketoacid to form acetolactate or acetohydroxybutyrate as products. Whereas the
Biochimica et biophysica acta, 1245(3), 366-370 (1995-12-14)
Acetolactate nonenzymatically reduced flavins, quinones and nicotinamide coenzymes in a time-dependent manner at physiological pH and moderate temperature. In the presence of excess acetolactate, the reduction of FAD and NAD+ followed pseudo-first-order kinetics. The rate of reduction was proportional to
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